{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Devi S"],"funding":["NIH"],"pagination":["107435"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11259706"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(7)"],"pubmed_abstract":["The protein phosphatase 5 (PP5) is normally recruited to its substrates by the molecular chaperones, heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90). This interaction requires the tetratricopeptide repeat (TPR) domain of PP5, which binds to an EEVD motif at the extreme C termini of cytosolic Hsp70 and Hsp90 isoforms. In addition to bringing PP5 into proximity with chaperone-bound substrates, this interaction also relieves autoinhibition in PP5's catalytic domain, promoting its phosphatase activity. To better understand the molecular determinants of this process, we screened a large, pentapeptide library for binding to PP5. This screen identified the amino acid preferences at each position, which we validated by showing that the optimal sequences bind 4- to 7-fold tighter th"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Exploration of the binding determinants of protein phosphatase 5 (PP5) reveals a chaperone-independent activation mechanism."],"pmcid":["PMC11259706"],"funding_grant_id":["RF1AG068125","R01GM141299"],"pubmed_authors":["Charvat A","Vinueza N","Gestwicki JE","Devi S","Millbern Z"],"additional_accession":[]},"is_claimable":false,"name":"Exploration of the binding determinants of protein phosphatase 5 (PP5) reveals a chaperone-independent activation mechanism.","description":"The protein phosphatase 5 (PP5) is normally recruited to its substrates by the molecular chaperones, heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90). This interaction requires the tetratricopeptide repeat (TPR) domain of PP5, which binds to an EEVD motif at the extreme C termini of cytosolic Hsp70 and Hsp90 isoforms. In addition to bringing PP5 into proximity with chaperone-bound substrates, this interaction also relieves autoinhibition in PP5's catalytic domain, promoting its phosphatase activity. To better understand the molecular determinants of this process, we screened a large, pentapeptide library for binding to PP5. This screen identified the amino acid preferences at each position, which we validated by showing that the optimal sequences bind 4- to 7-fold tighter th","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2025-04-26T22:21:11.854Z","creation":"2025-04-06T17:13:02.455Z"},"accession":"S-EPMC11259706","cross_references":{"pubmed":["38830406"],"doi":["10.1016/j.jbc.2024.107435"]}}